Cdc15 (SPAC20G8.05c) is the founding member of the PCH/F-BAR (Pombe Cdc15 Homology) protein family and an essential membrane-cytoskeleton scaffolding protein required for cytokinesis in fission yeast. It has a three-part domain architecture: an N-terminal FCH/F-BAR membrane-binding module, a central intrinsically disordered region (IDR) that is uniquely essential and heavily phosphoregulated, and a C-terminal SH3 protein-interaction domain. Its core molecular role is to couple the plasma membrane to actomyosin contractile-ring components and regulators, thereby driving assembly, anchoring, and integrity of the contractile ring at the cell division site. The F-BAR domain binds membrane phospholipids and provides a protein-binding platform that directly recruits the formin Cdc12 (and type-I myosin Myo1), while the SH3 domain (partly redundant with the SH3 of the paralog Imp2) recruits ring-stabilizing proteins such as Pxl1 (paxillin) and Fic1. Cdc15 is hyperphosphorylated in interphase (localizing to cortical patches at cell tips) and becomes hypophosphorylated during mitosis/cytokinesis (relocalizing to the medial contractile ring); dephosphorylation (involving the Clp1/Cdc14-family phosphatase) promotes an assembly-competent open conformation, increased membrane binding, oligomerization, and phase separation, whereas multiple polarity kinases (Pom1, Kin1, Shk1/Pak1, Pck1) phosphorylate the IDR to antagonize condensation and ring assembly. Note that S. pombe Cdc15 is an F-BAR/SH3 scaffold and is NOT a protein kinase (unlike the unrelated budding-yeast Cdc15 of the Mitotic Exit Network).
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Cdc15 binds the plasma membrane via its F-BAR domain and acts at the cytoplasmic face of the plasma membrane, where it anchors the contractile ring. This localization is well supported and phosphoregulated. Reason: Core localization for an F-BAR membrane-binding scaffold; consistent with phospholipid binding and membrane-anchor activity annotations. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md couple the plasma membrane to contractile-ring components and regulators |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Cdc15 has a cytosolic pool, particularly in interphase, but its functionally relevant localizations are the cell tips (interphase) and the medial cortex/contractile ring (mitosis). The bare cytoplasm term is correct but uninformative relative to the specific cortical/ring localizations. Reason: Generic compartment; subsumed by more specific cortical and division-site localizations that capture the functional sites of action. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md Dephosphorylation correlates with relocalization from mainly cytosolic/interphase pools to the division site |
| GO:0032153 cell division site | IBA GO_REF:0000033 | ACCEPT | Summary: Cdc15 accumulates at the medial cortex/cell division site during mitosis/cytokinesis, where it scaffolds the contractile ring. This is a core localization. Reason: Core site of Cdc15 function; the contractile ring assembles and constricts at the cell division site. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md In **mitosis/cytokinesis**, it accumulates at the **medial cortex/contractile ring** |
| GO:0007010 cytoskeleton organization | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Cdc15 organizes the actomyosin contractile ring, a cytoskeletal structure. The specific term mitotic actomyosin contractile ring assembly (GO:1903475) captures this more precisely; the generic parent is retained as non-core. Reason: General parent process; the specific contractile-ring assembly term is the core biological process. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md assembly, anchoring, and integrity of the actomyosin contractile ring |
| GO:0005543 phospholipid binding | IBA GO_REF:0000033 | ACCEPT | Summary: The Cdc15 F-BAR domain binds membrane phospholipids; its concave surface engages the membrane while the opposite surface binds protein ligands. This is a core molecular function of the F-BAR scaffold. Reason: Direct membrane phospholipid binding by the F-BAR domain is a core molecular function underlying membrane anchoring. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md The **concave F-BAR surface** binds membranes, while the **opposite surface** binds protein ligands |
| GO:0120104 mitotic actomyosin contractile ring, proximal layer | IBA GO_REF:0000033 | ACCEPT | Summary: Nanoscale architecture studies place Cdc15 in the membrane-proximal layer of the contractile ring, consistent with its role linking the ring to the plasma membrane. This is a precise and appropriate localization. Reason: Cdc15 is a membrane-proximal ring component that anchors the ring to the plasma membrane. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md physically linking the ring to the plasma membrane |
| GO:0005543 phospholipid binding | IEA GO_REF:0000117 | ACCEPT | Summary: F-BAR-mediated phospholipid binding is supported experimentally and by domain inference; consistent with the IBA annotation to the same term. Reason: Core molecular function; matches experimentally supported F-BAR membrane binding. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md a dimeric/oligomeric membrane-binding module |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Cdc15 associates with the actomyosin contractile ring (a cytoskeletal structure). The specific contractile-ring CC terms (GO:0110085, GO:0120104) are more informative; the generic parent is non-core. Reason: Overly general; specific contractile-ring localizations capture the functional site. |
| GO:0106006 cytoskeletal protein-membrane anchor activity | IEA GO_REF:0000117 | ACCEPT | Summary: This is the central molecular function of Cdc15: it couples the plasma membrane to the actomyosin contractile ring, linking a cytoskeletal structure to the membrane via its F-BAR domain. Strongly supported across multiple lines of evidence. Reason: Core molecular function of the F-BAR scaffold; membrane-cytoskeleton anchoring. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md couple the plasma membrane to contractile-ring components and regulators |
| GO:0120104 mitotic actomyosin contractile ring, proximal layer | IEA GO_REF:0000117 | ACCEPT | Summary: Cdc15 occupies the membrane-proximal layer of the contractile ring; consistent with the IBA and IDA annotations to this term. Reason: Core membrane-proximal ring localization. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md physically linking the ring to the plasma membrane |
| GO:1903475 mitotic actomyosin contractile ring assembly | IEA GO_REF:0000117 | ACCEPT | Summary: Cdc15 is an early, abundant contractile-ring component essential for ring assembly; it provides a membrane-associated scaffold that recruits and organizes the ring machinery (including the formin Cdc12). This is a core biological process. Reason: Core biological process; Cdc15 drives contractile-ring assembly. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md early and abundant** contractile-ring component and is **essential for cytokinesis** |
| GO:0005515 protein binding | IPI PMID:12939254 The PCH family protein, Cdc15p, recruits two F-actin nucleat... | MARK AS OVER ANNOTATED | Summary: Cdc15 directly binds multiple ring proteins (formin Cdc12, type-I myosin Myo1, Pxl1, Fic1) via its F-BAR and SH3 domains, coordinating two F-actin nucleation pathways for ring formation. While the underlying interactions are real and important, the bare protein binding term is uninformative and is better captured by the membrane-anchor activity and specific recruitment annotations. Reason: The bare protein binding term is uninformative; the specific scaffolding/recruitment functions are captured by GO:0106006 and the contractile-ring assembly terms. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md implicated as recruited via the F-BAR region in the prevailing model of medial F-actin nucleation factor recruitment |
| GO:0005515 protein binding | IPI PMID:19474789 A spatial gradient coordinates cell size and mitotic entry i... | MARK AS OVER ANNOTATED | Summary: Generic protein-binding annotation. Cdc15 relevant interactions (e.g., with polarity kinases and ring components) are better represented by specific molecular-function and process terms. Reason: Uninformative protein binding; superseded by specific functional terms. |
| GO:0106006 cytoskeletal protein-membrane anchor activity | EXP PMID:15933715 Etd1p is a novel protein that links the SIN cascade with cyt... | ACCEPT | Summary: Experimental support for Cdc15 acting as a membrane-cytoskeleton anchor at the division site; consistent with the core molecular function. Reason: Core molecular function with experimental support. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md membrane–cytoskeleton scaffolding protein |
| GO:0005515 protein binding | IPI PMID:35108037 Fission yeast paxillin contains two Cdc15 binding motifs for... | MARK AS OVER ANNOTATED | Summary: This annotation reflects the direct Cdc15-Pxl1 (paxillin) interaction; Pxl1 contains two Cdc15-binding motifs for robust recruitment to the ring. The specific interaction is captured by membrane-anchor/recruitment terms; the bare protein binding term is uninformative. Reason: Uninformative protein binding; the Pxl1 recruitment role is captured by the membrane-anchor and ring-assembly annotations. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md recruited via SH3 domains of Cdc15 and Imp2 |
| GO:0061171 establishment of bipolar cell polarity | IMP PMID:23093943 Cytokinesis-based constraints on polarized cell growth in fi... | KEEP AS NON CORE | Summary: Cdc15 localizes to cell tips in interphase and cytokinesis imposes constraints on polarized growth (new-end take-off), but bipolar polarity establishment is a downstream/pleiotropic consequence rather than Cdc15 core cytokinetic scaffolding function. Reason: Pleiotropic developmental/polarity process secondary to the core cytokinesis function. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md cortical patches at the cell tips |
| GO:0106006 cytoskeletal protein-membrane anchor activity | IPI PMID:23093943 Cytokinesis-based constraints on polarized cell growth in fi... | ACCEPT | Summary: Membrane-anchor molecular function supported by interaction evidence; consistent with the core function of Cdc15. Reason: Core molecular function. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md couple the plasma membrane to contractile-ring components and regulators |
| GO:0106006 cytoskeletal protein-membrane anchor activity | EXP PMID:32101481 DYRK kinase Pom1 drives F-BAR protein Cdc15 from the membran... | ACCEPT | Summary: Pom1 (a DYRK-family kinase) phosphorylates Cdc15 to drive it from the membrane, regulating the membrane-anchor function; the underlying anchor activity is core. Reason: Core molecular function; phosphoregulation modulates membrane association. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md Multiple kinases contribute (Pom1, Kin1, Shk1/Pak1, Pck1) |
| GO:0106006 cytoskeletal protein-membrane anchor activity | EXP PMID:25428987 The Cdc15 and Imp2 SH3 domains cooperatively scaffold a netw... | ACCEPT | Summary: The Cdc15 and Imp2 SH3 domains cooperatively scaffold a network of ring proteins; the membrane-anchor activity is the core molecular function. Reason: Core molecular function with experimental support. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md SH3 domains of Cdc15 and Imp2 cooperatively recruit Pxl1 and Fic1 |
| GO:0106006 cytoskeletal protein-membrane anchor activity | IMP PMID:24127216 The formins Cdc12 and For3 cooperate during contractile ring... | ACCEPT | Summary: Cdc15-dependent recruitment of the formin Cdc12 (cooperating with For3) for ring assembly relies on the membrane-anchor scaffold function. Reason: Core molecular function. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md Cdc15 directly binds Cdc12, and Cdc12 binding is phosphorylation-state dependent |
| GO:0106006 cytoskeletal protein-membrane anchor activity | EXP PMID:33357436 Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membran... | ACCEPT | Summary: Structural work shows opposite surfaces of the Cdc15 F-BAR create a membrane platform: the concave surface binds membrane, the opposite surface binds protein ligands (e.g., Cdc12). This directly demonstrates the membrane-anchor molecular function. Reason: Core molecular function directly demonstrated structurally. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md Cdc15 F-BAR domain contains a defined Cdc12-binding surface with micromolar affinity |
| GO:0106006 cytoskeletal protein-membrane anchor activity | IDA PMID:33357436 Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membran... | ACCEPT | Summary: Direct assay support for the F-BAR membrane platform that coordinates cytoskeletal and signaling components; core molecular function. Reason: Core molecular function directly assayed. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md The **concave F-BAR surface** binds membranes, while the **opposite surface** binds protein ligands |
| GO:0106006 cytoskeletal protein-membrane anchor activity | IMP PMID:26702831 Oligomerization but Not Membrane Bending Underlies the Funct... | ACCEPT | Summary: Mutational analysis shows oligomerization (not membrane bending) underlies Cdc15 function; the membrane-anchor activity remains core. F-BAR oligomerization is important for stable ring architecture. Reason: Core molecular function; oligomerization-dependent membrane anchoring. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md F-BAR oligomerization is important for stable ring architecture |
| GO:0106006 cytoskeletal protein-membrane anchor activity | EXP PMID:25688133 The F-BAR Cdc15 promotes contractile ring formation through ... | ACCEPT | Summary: The F-BAR Cdc15 promotes ring formation through direct recruitment of the formin Cdc12 to the membrane; this depends on the membrane-anchor scaffold function. Reason: Core molecular function with experimental support. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md recruiting factors (including the formin Cdc12) and physically linking the ring to the plasma membrane |
| GO:0005515 protein binding | IPI PMID:24790095 Characterization of the roles of Blt1p in fission yeast cyto... | MARK AS OVER ANNOTATED | Summary: Reflects an interaction detected in studies of Blt1 (a ring/node component). Generic protein binding is uninformative relative to the specific scaffolding functions. Reason: Uninformative protein binding; superseded by specific functional terms. |
| GO:0032178 medial membrane band | IDA PMID:31276301 A unique kinesin-like protein, Klp8, is involved in mitosis ... | ACCEPT | Summary: Cdc15 localizes to the medial membrane band at the division site, consistent with its membrane-proximal contractile-ring localization. Reason: Core medial division-site localization. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md it accumulates at the **medial cortex/contractile ring** |
| GO:0005515 protein binding | IPI PMID:23615450 Separate roles of IQGAP Rng2p in forming and constricting th... | MARK AS OVER ANNOTATED | Summary: Reflects interaction with the IQGAP Rng2, a node/ring component detected in the Cdc15 phosphorylation-dependent interactome. Generic protein binding is uninformative. Reason: Uninformative protein binding; the Rng2 interaction is captured by the ring-assembly and anchor annotations. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md Additional partners detected in a phosphorylation-dependent interactome context include **Cyk3** and **Rng2** |
| GO:0071341 medial cortical node | IDA PMID:16864655 Assembly of the cytokinetic contractile ring from a broad ba... | ACCEPT | Summary: The contractile ring assembles from a broad band of medial cortical nodes; Cdc15 is a node/ring component. This is a core localization. Reason: Core localization; nodes are precursors of the contractile ring. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md helps recruit and organize ring machinery |
| GO:0110085 mitotic actomyosin contractile ring | IDA PMID:16864655 Assembly of the cytokinetic contractile ring from a broad ba... | ACCEPT | Summary: Cdc15 is a bona fide component of the mitotic actomyosin contractile ring; directly observed at the ring. Core localization. Reason: Core localization; Cdc15 is an integral contractile-ring component. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md early and abundant** contractile-ring component |
| GO:0005543 phospholipid binding | IDA PMID:26702831 Oligomerization but Not Membrane Bending Underlies the Funct... | ACCEPT | Summary: Direct assay support for Cdc15 F-BAR phospholipid binding; core molecular function. Reason: Core molecular function directly assayed. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md a dimeric/oligomeric membrane-binding module |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:26702831 Oligomerization but Not Membrane Bending Underlies the Funct... | ACCEPT | Summary: Cdc15 acts on the cytoplasmic (inner) face of the plasma membrane, where its F-BAR domain binds the membrane and anchors the ring. Precise and core localization. Reason: Core localization; the F-BAR binds the inner leaflet of the plasma membrane. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md The **concave F-BAR surface** binds membranes |
| GO:0032153 cell division site | IDA PMID:26702831 Oligomerization but Not Membrane Bending Underlies the Funct... | ACCEPT | Summary: Direct observation of Cdc15 at the cell division site; core localization. Reason: Core site of Cdc15 function. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md scaffolding at the division site |
| GO:0097753 membrane bending | IMP NOT PMID:26702831 Oligomerization but Not Membrane Bending Underlies the Funct... | ACCEPT | Summary: This is a NOT annotation. Although F-BAR proteins are canonically associated with membrane curvature, the study demonstrates that oligomerization, NOT membrane bending, underlies Cdc15 function in cytokinesis. The negation is therefore correct: Cdc15 does not require membrane-bending activity for its essential cytokinetic role. Reason: The negation is correct and informative; oligomerization rather than membrane bending underlies Cdc15 function. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md F-BAR oligomerization is important for stable ring architecture |
| GO:0110085 mitotic actomyosin contractile ring | IDA PMID:16687577 Cell cycle-dependent roles for the FCH-domain protein Cdc15p... | ACCEPT | Summary: Cell-cycle-dependent imaging directly places Cdc15 at the actomyosin ring during mitosis; core localization. Reason: Core localization; integral contractile-ring component. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md medial contractile ring during mitosis |
| GO:1903475 mitotic actomyosin contractile ring assembly | IGI PMID:16687577 Cell cycle-dependent roles for the FCH-domain protein Cdc15p... | ACCEPT | Summary: Genetic interaction evidence that Cdc15 is required for actomyosin ring formation; core biological process. Reason: Core biological process; Cdc15 is essential for ring assembly. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md early and abundant** contractile-ring component and is **essential for cytokinesis** |
| GO:1903475 mitotic actomyosin contractile ring assembly | IMP PMID:25688133 The F-BAR Cdc15 promotes contractile ring formation through ... | ACCEPT | Summary: Cdc15 promotes ring formation through direct recruitment of the formin Cdc12; core biological process. Reason: Core biological process with mutant-phenotype support. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md recruiting factors (including the formin Cdc12) and physically linking the ring to the plasma membrane |
| GO:0106006 cytoskeletal protein-membrane anchor activity | IPI PMID:29343550 Cdk1-dependent phosphoinhibition of a formin-F-BAR interacti... | ACCEPT | Summary: Cdk1-dependent phosphoinhibition of the formin-F-BAR (Cdc12-Cdc15) interaction regulates ring formation; the underlying anchor/recruitment activity is core. Reason: Core molecular function; phosphoregulated Cdc12 recruitment. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md hypophosphorylated Cdc15 binds; hyperphosphorylated binds poorly |
| GO:1903475 mitotic actomyosin contractile ring assembly | EXP PMID:29343550 Cdk1-dependent phosphoinhibition of a formin-F-BAR interacti... | ACCEPT | Summary: Phosphoregulation of the Cdc12-Cdc15 interaction opposes contractile-ring formation; core biological process. Reason: Core biological process. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md Cdc12 binding is phosphorylation-state dependent |
| GO:0071341 medial cortical node | IDA PMID:21422229 Assembly and architecture of precursor nodes during fission ... | ACCEPT | Summary: Cdc15 is part of precursor nodes that assemble into the contractile ring; core localization. Reason: Core localization; nodes are ring precursors. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md helps recruit and organize ring machinery |
| GO:0030479 actin cortical patch | IDA PMID:21885283 Distinct roles for F-BAR proteins Cdc15p and Bzz1p in actin ... | KEEP AS NON CORE | Summary: Cdc15 (with Bzz1) has a distinct role in actin polymerization at sites of endocytosis, localizing to actin cortical patches. This endocytic role is a genuine but non-core moonlighting function relative to its essential cytokinetic scaffolding. Reason: Endocytosis-associated cortical-patch localization is a secondary function distinct from the core cytokinetic role. |
| GO:0072583 clathrin-dependent endocytosis | IMP PMID:21885283 Distinct roles for F-BAR proteins Cdc15p and Bzz1p in actin ... | KEEP AS NON CORE | Summary: Cdc15 contributes to actin polymerization at endocytic sites alongside the F-BAR protein Bzz1. This is a non-core function distinct from the essential cytokinetic scaffolding role. Reason: Moonlighting endocytic function; not the core cytokinesis role. |
| GO:0110085 mitotic actomyosin contractile ring | IDA PMID:21885283 Distinct roles for F-BAR proteins Cdc15p and Bzz1p in actin ... | ACCEPT | Summary: Cdc15 directly observed at the contractile ring; core localization. Reason: Core localization; integral ring component. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md medial cortex/contractile ring |
| GO:0120104 mitotic actomyosin contractile ring, proximal layer | IDA PMID:28914606 Nanoscale architecture of the Schizosaccharomyces pombe cont... | ACCEPT | Summary: Nanoscale architecture analysis directly places Cdc15 in the membrane-proximal layer of the contractile ring; core localization. Reason: Core membrane-proximal ring localization, directly observed. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md physically linking the ring to the plasma membrane |
| GO:0106006 cytoskeletal protein-membrane anchor activity | IPI PMID:19139265 The SH3 domains of two PCH family members cooperate in assem... | ACCEPT | Summary: The SH3 domains of two PCH family members (Cdc15 and Imp2) cooperate in assembling the contractile ring; the membrane-anchor activity is core. Reason: Core molecular function. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md partly **redundant with the SH3 domain of the paralog Imp2** |
| GO:0106006 cytoskeletal protein-membrane anchor activity | IMP PMID:28784611 Phosphoinositide-mediated ring anchoring resists perpendicul... | ACCEPT | Summary: Phosphoinositide-mediated ring anchoring resists perpendicular forces to promote medial cytokinesis; the Cdc15 membrane-anchor activity is central to this mechanical anchoring. Reason: Core molecular function; mechanical anchoring of the ring to the membrane. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md Coupling membrane remodeling and cytoskeletal force generation |
| GO:0030479 actin cortical patch | IDA PMID:14602073 Spatial and temporal pathway for assembly and constriction o... | KEEP AS NON CORE | Summary: Cdc15 observed at actin cortical patches; consistent with its endocytosis- associated localization. Non-core relative to the cytokinetic scaffold role. Reason: Cortical-patch localization tied to the non-core endocytic function. |
| GO:0110085 mitotic actomyosin contractile ring | IDA PMID:14602073 Spatial and temporal pathway for assembly and constriction o... | ACCEPT | Summary: Spatiotemporal pathway analysis directly places Cdc15 at the contractile ring during assembly and constriction; core localization. Reason: Core localization; integral ring component. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md early and abundant** contractile-ring component |
| GO:0110085 mitotic actomyosin contractile ring | IDA PMID:18378776 The Clp1/Cdc14 phosphatase contributes to the robustness of ... | ACCEPT | Summary: Cdc15 at the contractile ring in the context of Clp1/Cdc14 phosphatase and Mid1; core localization. Reason: Core localization; integral ring component. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md medial contractile ring during mitosis |
| GO:0005515 protein binding | IPI PMID:26702831 Oligomerization but Not Membrane Bending Underlies the Funct... | MARK AS OVER ANNOTATED | Summary: Generic protein-binding annotation arising from interaction assays in the oligomerization study. The functional interactions are captured by the membrane-anchor and ring annotations. Reason: Uninformative protein binding; superseded by specific functional terms. |
| GO:1903475 mitotic actomyosin contractile ring assembly | IMP PMID:26702831 Oligomerization but Not Membrane Bending Underlies the Funct... | ACCEPT | Summary: Cdc15 oligomerization underlies its function in contractile-ring assembly; core biological process. Reason: Core biological process. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md F-BAR oligomerization is important for stable ring architecture |
| GO:0110085 mitotic actomyosin contractile ring | IDA PMID:24790095 Characterization of the roles of Blt1p in fission yeast cyto... | ACCEPT | Summary: Cdc15 at the contractile ring in the context of Blt1 characterization; core localization. Reason: Core localization; integral ring component. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md medial cortex/contractile ring |
| GO:0043332 mating projection tip | IDA PMID:25825517 A formin-nucleated actin aster concentrates cell wall hydrol... | KEEP AS NON CORE | Summary: During mating/cell fusion, a formin-nucleated actin aster concentrates cell wall hydrolases; Cdc15 localizes to the mating projection (fusion focus) tip. This is a non-core, context-specific localization distinct from the core cytokinetic role. Reason: Mating/fusion-specific localization; not the core cytokinesis function. |
| GO:0005737 cytoplasm | IDA PMID:7634333 The S. pombe cdc15 gene is a key element in the reorganizati... | KEEP AS NON CORE | Summary: Early characterization of the cdc15 gene noted a cytoplasmic pool. The functionally relevant localizations are the cortical/division-site pools. Reason: Generic compartment; subsumed by specific cortical/ring localizations. |
| GO:0032153 cell division site | IDA PMID:7634333 The S. pombe cdc15 gene is a key element in the reorganizati... | ACCEPT | Summary: The original cdc15 study showed it is key to F-actin reorganization at mitosis at the division site; core localization. Reason: Core site of Cdc15 function. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md scaffolding at the division site |
| GO:1903475 mitotic actomyosin contractile ring assembly | IMP PMID:7634333 The S. pombe cdc15 gene is a key element in the reorganizati... | ACCEPT | Summary: Loss of cdc15 disrupts F-actin reorganization required for ring formation at mitosis; core biological process. Reason: Core biological process; founding evidence for the Cdc15 cytokinetic role. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md essential for cytokinesis |
| GO:0005515 protein binding | IPI PMID:25428987 The Cdc15 and Imp2 SH3 domains cooperatively scaffold a netw... | MARK AS OVER ANNOTATED | Summary: Generic protein-binding annotation from the SH3-domain interaction-network study; the specific SH3-mediated recruitment of Pxl1/Fic1 is captured by the anchor and ring-assembly annotations. Reason: Uninformative protein binding; superseded by specific functional terms. |
| GO:0032153 cell division site | IDA PMID:25428987 The Cdc15 and Imp2 SH3 domains cooperatively scaffold a netw... | ACCEPT | Summary: Cdc15 at the cell division site in the SH3-network study; core localization. Reason: Core site of Cdc15 function. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md scaffolding at the division site |
| GO:0110085 mitotic actomyosin contractile ring | IDA PMID:25428987 The Cdc15 and Imp2 SH3 domains cooperatively scaffold a netw... | ACCEPT | Summary: Cdc15 at the contractile ring; core localization. Reason: Core localization; integral ring component. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md medial cortex/contractile ring |
| GO:1903475 mitotic actomyosin contractile ring assembly | IGI PMID:25428987 The Cdc15 and Imp2 SH3 domains cooperatively scaffold a netw... | ACCEPT | Summary: Cdc15 and Imp2 SH3 domains redundantly ensure efficient cell division; combined loss abolishes ring formation. Core biological process. Reason: Core biological process; SH3-mediated scaffolding ensures ring assembly. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md Combined loss of Cdc15/Imp2 SH3 functions abolishes ring formation |
| GO:0005515 protein binding | IPI PMID:23966468 Cooperation between Rho-GEF Gef2 and its binding partner Nod... | MARK AS OVER ANNOTATED | Summary: Reflects interaction in the Gef2-Nod1 cytokinesis-regulation network. Generic protein binding is uninformative. Reason: Uninformative protein binding; superseded by specific functional terms. |
| GO:1903475 mitotic actomyosin contractile ring assembly | IMP PMID:24127216 The formins Cdc12 and For3 cooperate during contractile ring... | ACCEPT | Summary: The formins Cdc12 and For3 cooperate during ring assembly downstream of Cdc15-mediated Cdc12 recruitment; core biological process. Reason: Core biological process. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md recruiting factors (including the formin Cdc12) |
| GO:1903475 mitotic actomyosin contractile ring assembly | IMP PMID:19139265 The SH3 domains of two PCH family members cooperate in assem... | ACCEPT | Summary: SH3-domain cooperation between Cdc15 and Imp2 drives contractile-ring assembly; core biological process. Reason: Core biological process. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md SH3 domains of Cdc15 and Imp2 cooperatively recruit Pxl1 and Fic1 |
| GO:0032153 cell division site | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: High-throughput localization (ORFeome) places Cdc15 at the cell division site; consistent with directed studies. Core localization. Reason: Core site of Cdc15 function (corroborated by directed studies). Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md scaffolding at the division site |
| GO:0051286 cell tip | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: In interphase Cdc15 localizes to cortical patches at the cell tips; the high-throughput cell-tip localization is consistent with directed imaging. Reason: Core interphase localization at cell tips. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md cortical patches at the cell tips |
| GO:0032178 medial membrane band | IDA PMID:15517003 Organization of a sterol-rich membrane domain by cdc15p duri... | ACCEPT | Summary: Cdc15 organizes a sterol-rich membrane domain during cytokinesis, consistent with localization to the medial membrane band at the division site. Reason: Core medial division-site membrane localization. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md medial cortex/contractile ring |
| GO:0032153 cell division site | IDA PMID:9786952 imp2, a new component of the actin ring in the fission yeast... | ACCEPT | Summary: Study of imp2 (the Cdc15 paralog) places Cdc15 at the actin ring/division site; core localization. Reason: Core site of Cdc15 function. Supporting Evidence: file:SCHPO/cdc15/cdc15-deep-research-falcon.md scaffolding at the division site |
| GO:0005737 cytoplasm | HDA PMID:10759889 Large-scale screening of intracellular protein localization ... | KEEP AS NON CORE | Summary: Large-scale GFP-fusion localization detected a cytoplasmic pool. Generic compartment; functionally relevant pools are cortical/division-site. Reason: Generic compartment from high-throughput screen; subsumed by specific localizations. |
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Download this section (compressed HTML)Q: What is the precise in vivo contribution of Cdc15 liquid-liquid phase separation (condensate formation) versus classical oligomerization to contractile-ring assembly and stability?
Q: How is the combinatorial multisite phosphorylation code (Pom1, Kin1, Shk1/Pak1, Pck1) integrated to set the threshold for the Cdc15 closed-to-open conformational switch at mitotic onset?
Experiment: Use phosphomutant and IDR-deletion alleles combined with live-cell imaging and quantitative FRAP to measure how Cdc15 condensation/oligomerization state controls the recruitment dynamics of Cdc12, Myo1, Pxl1, and Fic1 at the ring.
Experiment: Reconstitute Cdc15 F-BAR on supported lipid bilayers with purified Cdc12 and Pxl1 peptides to quantify how phosphorylation state tunes simultaneous membrane binding and partner recruitment (membrane-platform function) in vitro.
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